2q8p

Crystal Structure of selenomethionine labelled S. aureus IsdE complexed with heme

spinqualitylabelsall models 2q8p, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2q8p is a 1 chain structure with sequence from Staan. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM NonStd Res: MSE Related: 2q8q Gene: isdE (STAAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ISDE_STAAN] Involved in heme (porphyrin) scavenging. Binds Fe(2+) and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a high-affinity heme binding protein and probably has a role in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Staphylococcus aureus is a Gram-positive bacterial pathogen and a leading cause of hospital acquired infections. Because the free iron concentration in the human body is too low to support growth, S. aureus must acquire iron from host sources. Heme iron is the most prevalent iron reservoir in the human body and a predominant source of iron for S. aureus. The iron-regulated surface determinant (Isd) system removes heme from host heme proteins and transfers it to IsdE, the cognate substrate-binding lipoprotein of an ATP-binding cassette transporter, for import and subsequent degradation. Herein, we report the crystal structure of the soluble portion of the IsdE lipoprotein in complex with heme. The structure reveals a bi-lobed topology formed by an N- and C-terminal domain bridged by a single alpha-helix. The structure places IsdE as a member of the helical backbone metal receptor superfamily. A six-coordinate heme molecule is bound in the groove established at the domain interface, and the heme iron is coordinated in a novel fashion for heme transporters by Met(78) and His(229). Both heme propionate groups are secured by H-bonds to IsdE main chain and side chain groups. Of these residues, His(229) is essential for IsdE-mediated heme uptake by S. aureus when growth on heme as a sole iron source is measured. Multiple sequence alignments of homologues from several other Gram-positive bacteria, including the human pathogens pyogenes, Bacillus anthracis, and Listeria monocytogenes, suggest that these other systems function equivalently to S. aureus IsdE with respect to heme binding and transport. Heme coordination by Staphylococcus aureus IsdE.,Grigg JC, Vermeiren CL, Heinrichs DE, Murphy ME J Biol Chem. 2007 Sep 28;282(39):28815-22. Epub 2007 Jul 31. PMID:17666394 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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